DUSP18 Human

DUSP18 is a protein encoded by the DUSP18 gene in humans. The recombinant form of this protein is often produced in Escherichia coli (E. coli) and is typically tagged with a His-tag for purification purposes. The amino acid sequence of the human recombinant DUSP18 includes 188 residues, and the protein has a theoretical molecular weight of approximately 23.6 kDa .

The protein contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the mitogen-activated protein kinase phosphatase (MKP) class of DUSPs . This structural configuration allows DUSP18 to specifically target and dephosphorylate its substrates.

DUSP18 exhibits preferential enzymatic activity against phosphorylated tyrosine residues over threonine residues. It is capable of dephosphorylating single and diphosphorylated synthetic MAPK peptides, with a higher affinity for the phosphotyrosine and diphosphorylated forms compared to phosphothreonine . Additionally, DUSP18 can dephosphorylate p-nitrophenyl phosphate (pNPP) in vitro .

The activity of DUSP18 is inhibited by iodoacetic acid and is activated by manganese ions . This regulation of activity is essential for its function in various cellular signaling pathways.

Dual-specificity phosphatases, including DUSP18, are major modulators of critical signaling pathways. They play a significant role in cellular processes such as cell growth, differentiation, and apoptosis. By dephosphorylating key signaling molecules, DUSP18 helps maintain the balance of phosphorylation states within the cell, which is crucial for proper cellular function .

Recombinant human DUSP18 is widely used in research to study its role in cellular signaling and its potential implications in various diseases. The availability of recombinant forms allows researchers to investigate the enzyme’s activity, regulation, and interactions with other proteins in a controlled environment.